메뉴 건너뛰기




Volumn 49, Issue 2, 2011, Pages 257-264

A Thermostable phytase from Neosartorya spinosa BCC 41923 and its expression in Pichia pastoris

Author keywords

enzyme characterization; gene cloning; Neosartorya spinosa; phytase; Pichia pastoris

Indexed keywords

PHYTASE; PHYTIC ACID; RECOMBINANT PROTEIN;

EID: 79955720112     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-011-0369-x     Document Type: Article
Times cited : (19)

References (36)
  • 1
    • 8344239556 scopus 로고    scopus 로고
    • Metabolism of extracellular inositol hexaphosphate (phytase) by Saccharomyces cerevisiae
    • Andlid, T. A., J. Veide, and A. S. Sandberg. 2004. Metabolism of extracellular inositol hexaphosphate (phytase) by Saccharomyces cerevisiae. Int. J. Food Microbiol. 97, 157-169.
    • (2004) Int. J. Food Microbiol. , vol.97 , pp. 157-169
    • Andlid, T.A.1    Veide, J.2    Sandberg, A.S.3
  • 2
    • 34848899829 scopus 로고    scopus 로고
    • Purification and characterisation of an acid phosphatase with phytase activity from Mucor hiemalis Wehmer
    • Boyce, A. and G. Walsh. 2007. Purification and characterisation of an acid phosphatase with phytase activity from Mucor hiemalis Wehmer. J. Biotechnol. 132, 82-87.
    • (2007) J. Biotechnol. , vol.132 , pp. 82-87
    • Boyce, A.1    Walsh, G.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0346139366 scopus 로고
    • Ovalbumin gene: evidence for a leader sequence in mRNA and DNA sequences at the exon-intron boundaries
    • Breathnach, R., C. Benoist, K. O'Hare, F. Gannon, and P. Chambon. 1978. Ovalbumin gene: evidence for a leader sequence in mRNA and DNA sequences at the exon-intron boundaries. Proc. Natl. Acad. Sci. USA 75, 4853-4857.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4853-4857
    • Breathnach, R.1    Benoist, C.2    O'Hare, K.3    Gannon, F.4    Chambon, P.5
  • 5
    • 14644388886 scopus 로고    scopus 로고
    • Phytase activity from Aspergillus oryzae AK9 cultivated on solid state soybean meal medium
    • Chantasartrasamee, K., D. Israngkul, S. Intarareugsorn, and S. Dharmsthiti. 2005. Phytase activity from Aspergillus oryzae AK9 cultivated on solid state soybean meal medium. Proc. Biochem. 40, 2285-2289.
    • (2005) Proc. Biochem. , vol.40 , pp. 2285-2289
    • Chantasartrasamee, K.1    Israngkul, D.2    Intarareugsorn, S.3    Dharmsthiti, S.4
  • 6
    • 0031307229 scopus 로고    scopus 로고
    • Characterization of phytase produced by Aspergillus niger
    • Dvoráková, J., O. Volfová, and J. Kopecky. 1997. Characterization of phytase produced by Aspergillus niger. Folia Microbiol. 42, 349-352.
    • (1997) Folia Microbiol , vol.42 , pp. 349-352
    • Dvoráková, J.1    Volfová, O.2    Kopecky, J.3
  • 8
    • 0037415282 scopus 로고    scopus 로고
    • Effect of culture conditions on the biosynthesis of Aspergillus niger phytase and acid phosphatase
    • Gargova, S. and M. Sariyska. 2003. Effect of culture conditions on the biosynthesis of Aspergillus niger phytase and acid phosphatase. Enzym. Microb. Technol. 32, 231-235.
    • (2003) Enzym. Microb. Technol. , vol.32 , pp. 231-235
    • Gargova, S.1    Sariyska, M.2
  • 9
    • 0000337911 scopus 로고
    • Calcium binding to phytic acid
    • Graf, E. 1983. Calcium binding to phytic acid. J. Agric. Food Chem. 31, 851-855.
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 851-855
    • Graf, E.1
  • 10
    • 33847312304 scopus 로고    scopus 로고
    • Recombinant production of Penicillium oxalicum PJ3 phytase in Pichia pastoris
    • Lee, J., Y. Choi, P. C. Lee, S. Kang, J. Bok, and J. Cho. 2007. Recombinant production of Penicillium oxalicum PJ3 phytase in Pichia pastoris. World J. Microbiol. Biotechnol. 23, 443-446.
    • (2007) World J. Microbiol. Biotechnol. , vol.23 , pp. 443-446
    • Lee, J.1    Choi, Y.2    Lee, P.C.3    Kang, S.4    Bok, J.5    Cho, J.6
  • 11
    • 0027273836 scopus 로고
    • Supplemental microbial phytase improves bioavailability of dietary zinc to weanling pigs
    • Lei, X., P. K. Ku, E. R. Miller, D. E. Ullrey, and M. T. Yokoyama. 1993. Supplemental microbial phytase improves bioavailability of dietary zinc to weanling pigs. J. Nutr. 123, 1117-1123.
    • (1993) J. Nutr. , vol.123 , pp. 1117-1123
    • Lei, X.1    Ku, P.K.2    Miller, E.R.3    Ullrey, D.E.4    Yokoyama, M.T.5
  • 12
    • 0031034203 scopus 로고    scopus 로고
    • The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila
    • Mitchell, D. B., K. Vogel, B. J. Weimann, L. Pasamontes, and A. P. van Loon. 1997. The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila. Microbiol. 143, 245-252.
    • (1997) Microbiol , vol.143 , pp. 245-252
    • Mitchell, D.B.1    Vogel, K.2    Weimann, B.J.3    Pasamontes, L.4    van Loon, A.P.5
  • 13
    • 0026495490 scopus 로고
    • A simple and efficient protocol for isolation of high molecular weight DNA from filamentous fungi, fruit bodies, and infected plant tissues
    • Möller, E. M., G. Bahnweg, H. Sandermann, and H. H. Geiger. 1992. A simple and efficient protocol for isolation of high molecular weight DNA from filamentous fungi, fruit bodies, and infected plant tissues. Nucleic Acids Res. 20, 6115-6116.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6115-6116
    • Möller, E.M.1    Bahnweg, G.2    Sandermann, H.3    Geiger, H.H.4
  • 15
    • 1642578253 scopus 로고    scopus 로고
    • Biochemical properties and substrate specificities of alkaline and histidine acid phytases
    • Oh, B. C., W. C. Choi, S. Park, Y. O. Kim, and T. K. Oh. 2004. Biochemical properties and substrate specificities of alkaline and histidine acid phytases. Appl. Microbiol. Biotechnol. 63, 362-372.
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 362-372
    • Oh, B.C.1    Choi, W.C.2    Park, S.3    Kim, Y.O.4    Oh, T.K.5
  • 17
    • 0030898612 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of a heat stable phytase from the fungus Aspergillus fumigatus
    • Pasamontes, L., M. Haiker, M. Wyss, M. Tessier, and A. P. G. M. van Loon. 1997. Gene cloning, purification, and characterization of a heat stable phytase from the fungus Aspergillus fumigatus. Appl. Environ. Microbiol. 63, 1696-1700.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1696-1700
    • Pasamontes, L.1    Haiker, M.2    Wyss, M.3    Tessier, M.4    van Loon, A.P.G.M.5
  • 18
    • 39549122561 scopus 로고    scopus 로고
    • Molecular gene cloning and overexpression of the phytase from Debaryomyces castellii CBS 2923
    • Ragon, M., V. Neugnot-Roux, P. Chemardin, G. Moulin, and H. Boze. 2008. Molecular gene cloning and overexpression of the phytase from Debaryomyces castellii CBS 2923. Protein Expr. Purif. 58, 275-283.
    • (2008) Protein Expr. Purif. , vol.58 , pp. 275-283
    • Ragon, M.1    Neugnot-Roux, V.2    Chemardin, P.3    Moulin, G.4    Boze, H.5
  • 20
    • 0034673345 scopus 로고    scopus 로고
    • Expression of the Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme
    • Rodriguez, E., E. J. Mullaney, and X. G. Lei. 2000. Expression of the Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme. Biochem. Biophys. Res. Commun. 268, 373-378.
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 373-378
    • Rodriguez, E.1    Mullaney, E.J.2    Lei, X.G.3
  • 21
    • 0033562103 scopus 로고    scopus 로고
    • Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro
    • Rodriguez, E., J. M. Porres, Y. M. Han, and X. G. Lei. 1999. Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) and Escherichia coli pH 2. 5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro. Arch. Biochem. Biophys. 365, 262-267.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 262-267
    • Rodriguez, E.1    Porres, J.M.2    Han, Y.M.3    Lei, X.G.4
  • 24
    • 57449117452 scopus 로고    scopus 로고
    • Characterization of a HAP-phytase from a thermophilic mould Sporotrichum thermophile
    • Singh, B. and T. Satyanarayana. 2009. Characterization of a HAP-phytase from a thermophilic mould Sporotrichum thermophile. Bioresour. Technol. 100, 2046-2051.
    • (2009) Bioresour. Technol. , vol.100 , pp. 2046-2051
    • Singh, B.1    Satyanarayana, T.2
  • 25
    • 0034577375 scopus 로고    scopus 로고
    • Isolation and characterization of novel phytase from Penicillium simplicissimum
    • Tseng, Y. H., T. J. Fang, and S. M. Tseng. 2000. Isolation and characterization of novel phytase from Penicillium simplicissimum. Folia Microbiol. 45, 121-127.
    • (2000) Folia Microbiol. , vol.45 , pp. 121-127
    • Tseng, Y.H.1    Fang, T.J.2    Tseng, S.M.3
  • 26
    • 33846471983 scopus 로고    scopus 로고
    • Express of Aspergillus oryzae phytase gene in Aspergillus oryzae RIB40 niaD-
    • Uchida, H., S. Arakida, T. Sakamoto, and H. Kawasaki. 2006. Express of Aspergillus oryzae phytase gene in Aspergillus oryzae RIB40 niaD-. J. Biosci. Bioeng. 102, 564-567.
    • (2006) J. Biosci. Bioeng. , vol.102 , pp. 564-567
    • Uchida, H.1    Arakida, S.2    Sakamoto, T.3    Kawasaki, H.4
  • 27
    • 0025787109 scopus 로고
    • Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytases
    • Ullah, A. H. J., B. J. Cummins, and H. C. Dischinger. 1991. Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytases. Biochem. Biophys. Res. Commun. 178, 45-53.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 45-53
    • Ullah, A.H.J.1    Cummins, B.J.2    Dischinger, H.C.3
  • 28
    • 0023080759 scopus 로고
    • Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: Purification and characterization
    • Ullah, A. H. J. and D. M. Gibson. 1987. Extracellular phytase (E. C. 3. 1. 3. 8) from Aspergillus ficuum NRRL 3135: Purification and characterization. Prep. Biochem. 17, 63-91.
    • (1987) Prep. Biochem. , vol.17 , pp. 63-91
    • Ullah, A.H.J.1    Gibson, D.M.2
  • 30
    • 34250649710 scopus 로고    scopus 로고
    • Cloning, expression, and enzyme characterization of an acid heat-stable phytase from Aspergillus fumigatus WY-2
    • Wang, Y., X. Gao, Q. Su, W. Wu, and L. An. 2007. Cloning, expression, and enzyme characterization of an acid heat-stable phytase from Aspergillus fumigatus WY-2. Curr. Microbiol. 55, 65-70.
    • (2007) Curr. Microbiol. , vol.55 , pp. 65-70
    • Wang, Y.1    Gao, X.2    Su, Q.3    Wu, W.4    An, L.5
  • 31
    • 33745859559 scopus 로고    scopus 로고
    • Purification, characterization, gene cloning and sequence analysis of a phytase from Klebsiella pneumoniae subsp. pneumoniae XY-5
    • Wang, X., S. Upatham, W. Panbangred, D. Isarangkul, P. Summpunn, S. Wiyakrutta, and V. Meevootisom. 2004. Purification, characterization, gene cloning and sequence analysis of a phytase from Klebsiella pneumoniae subsp. pneumoniae XY-5. Sci. Asia 30, 383-390.
    • (2004) Sci. Asia , vol.30 , pp. 383-390
    • Wang, X.1    Upatham, S.2    Panbangred, W.3    Isarangkul, D.4    Summpunn, P.5    Wiyakrutta, S.6    Meevootisom, V.7
  • 32
    • 0003899229 scopus 로고
    • Freehold, New Jersey, USA: Biochemical Products Division. Worthington Diagnostic System Inc
    • Worthington, T. M. 1982. Enzymes and related biochemicals. Biochemical Products Division. Worthington Diagnostic System Inc. Freehold, New Jersey, USA.
    • (1982) Enzymes and Related Biochemicals
    • Worthington, T.M.1
  • 34
    • 0031734945 scopus 로고    scopus 로고
    • Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase and A. niger pH 2.5 acid phosphatase
    • Wyss, M., L. Pasamontes, R. Rémy, J. Kohler, E. Kusznir, M. Gadient, F. Muller, and A. P. G. M van Loon. 1998. Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase and A. niger pH 2. 5 acid phosphatase. Appl. Environ. Microbiol. 64, 4446-4451.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4446-4451
    • Wyss, M.1    Pasamontes, L.2    Rémy, R.3    Kohler, J.4    Kusznir, E.5    Gadient, M.6    Muller, F.7    van Loon, A.P.G.M.8
  • 35
    • 3142666033 scopus 로고    scopus 로고
    • Isolation, characterization, and molecular cloning of the cDNA encoding a novel phytase from Aspergillus niger 113 and high expression in Pichia pastoris
    • Xiong, A. S., Q. H. Yao, R. H. Peng, X. Li, H. Q. Fan, M. J. Guo, and S. L. Zhang. 2004. Isolation, characterization, and molecular cloning of the cDNA encoding a novel phytase from Aspergillus niger 113 and high expression in Pichia pastoris. J. Biochem. Mol. Biol. 37, 282-291.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 282-291
    • Xiong, A.S.1    Yao, Q.H.2    Peng, R.H.3    Li, X.4    Fan, H.Q.5    Guo, M.J.6    Zhang, S.L.7
  • 36
    • 35448989797 scopus 로고    scopus 로고
    • Screening, cloning and overexpression of Aspergillus niger phytase (phyA) in Pichia pastoris with favourable characteristics
    • Zhao, D. M., M. Wang, X. J. Mu, M. L. Sun, and X. Y. Wang. 2007. Screening, cloning and overexpression of Aspergillus niger phytase (phyA) in Pichia pastoris with favourable characteristics. Lett. Appl. Microbiol. 45, 522-528.
    • (2007) Lett. Appl. Microbiol. , vol.45 , pp. 522-528
    • Zhao, D.M.1    Wang, M.2    Mu, X.J.3    Sun, M.L.4    Wang, X.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.